RiAFP: Difference between revisions

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Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>DOI 10.5772/54992</ref>. The longhorn beetle, ''Rhagium inquisitor'', has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (''Ri''AFP) in its hemolymph. <scene name='60/607864/Chain_a_without_histag/1'>~~''Ri''AFP~~</scene> is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.

Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>DOI 10.5772/54992</ref>. The longhorn beetle, ''Rhagium inquisitor'', has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (''Ri''AFP) in its hemolymph. <scene name='60/607864/Chain_a_without_histag/1'>RiAFP</scene> is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.

== Function ==

~~RiAFP~~, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10.1098/rsif.2014.0526</ref>. It is well accepted that AFPs inhibit ice crystals growth through the adsorption inhibition model<ref>DOI 10.1016/S0006-3495(91)82234-2</ref>. According to this model AFPs bind to an ice crystal surface and block water molecules from accessing it at the bound location. The ice front thus becomes convex toward the solution between the surface-bound AFPs, creating the microcurvature. Thus, the ice grow is less favorable due to Gibbs-Thompson-Herring (Kelvin) effect, which leads to noncolligative depression of the freezing point (Tf) of the solution (thermal hysteresis).

''Ri''AFP, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10.1098/rsif.2014.0526</ref>. It is well accepted that AFPs inhibit ice crystals growth through the adsorption inhibition model<ref>DOI 10.1016/S0006-3495(91)82234-2</ref>. According to this model AFPs bind to an ice crystal surface and block water molecules from accessing it at the bound location. The ice front thus becomes convex toward the solution between the surface-bound AFPs, creating the microcurvature. Thus, the ice grow is less favorable due to Gibbs-Thompson-Herring (Kelvin) effect, which leads to noncolligative depression of the freezing point (Tf) of the solution (thermal hysteresis).

== Overall Structure ==

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 <StructureSection load='4dt5' size='340' side='right' caption='Insect antifreeze protein  (PDB code [[4dt5]]).' scene='60/607864/Riafp_rocket/2'>
-Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>DOI 10.5772/54992</ref>. The longhorn beetle, ''Rhagium inquisitor'', has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (''Ri''AFP) in its hemolymph. <scene name='60/607864/Chain_a_without_histag/1'>''Ri''AFP</scene> is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.
+Antifreeze proteins (AFPs) evolved in various organisms permitting their survival in subzero environments<ref>PMID: 11852248</ref>. They exhibit remarkable structural diversity and molar activities across the various kingdoms<ref>DOI 10.5772/54992</ref>. The longhorn beetle, ''Rhagium inquisitor'', has the ability to supercool to below -25 °C partially due to the presence of a highly potent AFP (''Ri''AFP) in its hemolymph. <scene name='60/607864/Chain_a_without_histag/1'>RiAFP</scene> is a 13-kDa protein with one of the highest antifreeze activities measured for any AFP.
 == Function ==
-RiAFP, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10.1098/rsif.2014.0526</ref>. It is well accepted that AFPs inhibit ice crystals growth through the adsorption inhibition model<ref>DOI 10.1016/S0006-3495(91)82234-2</ref>. According to this model AFPs bind to an ice crystal surface and block water molecules from accessing it at the bound location. The ice front thus becomes convex toward the solution between the surface-bound AFPs, creating the microcurvature. Thus, the ice grow is less favorable due to Gibbs-Thompson-Herring (Kelvin) effect, which leads to noncolligative depression of the freezing point (Tf) of the solution (thermal hysteresis).
+''Ri''AFP, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10.1098/rsif.2014.0526</ref>. It is well accepted that AFPs inhibit ice crystals growth through the adsorption inhibition model<ref>DOI 10.1016/S0006-3495(91)82234-2</ref>. According to this model AFPs bind to an ice crystal surface and block water molecules from accessing it at the bound location. The ice front thus becomes convex toward the solution between the surface-bound AFPs, creating the microcurvature. Thus, the ice grow is less favorable due to Gibbs-Thompson-Herring (Kelvin) effect, which leads to noncolligative depression of the freezing point (Tf) of the solution (thermal hysteresis).
 == Overall Structure ==